scholarly journals Rab11 is required for cell adhesion, maintenance of cell shape and actin-cytoskeleton organization during Drosophila wing development

2011 ◽  
Vol 55 (3) ◽  
pp. 269-279 ◽  
Author(s):  
Tanmay Bhuin ◽  
Jagat K. Roy
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Cell Shape ◽  
Wing Development ◽  
Cytoskeleton Organization ◽  
Drosophila Wing ◽  
Actin Cytoskeleton Organization

scholarly journals Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation

Amino Acids ◽  
2014 ◽  
Vol 47 (1) ◽  
pp. 199-212 ◽  
Author(s):  
Iuliia Pavlyk ◽  
Yuriy Rzhepetskyy ◽  
Adam K. Jagielski ◽  
Jakub Drozak ◽  
Anna Wasik ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Glioblastoma Cell ◽  
Cytoskeleton Organization ◽  
Arginine Deprivation ◽  
Actin Cytoskeleton Organization

scholarly journals Cell adhesion is regulated by CDK1 during the cell cycle

2018 ◽  
Vol 217 (9) ◽  
pp. 3203-3218 ◽  
Author(s):  
Matthew C. Jones ◽  
Janet A. Askari ◽  
Jonathan D. Humphries ◽  
Martin J. Humphries
Keyword(s):  
Cell Cycle ◽  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Cell Cycle Progression ◽  
Cyclin B1 ◽  
Cycle Progression ◽  
Cytoskeleton Organization ◽  
Actin Cytoskeleton Organization ◽  
Dependent Growth ◽  
Adhesion Complex

In most tissues, anchorage-dependent growth and cell cycle progression are dependent on cells engaging extracellular matrices (ECMs) via integrin–receptor adhesion complexes. In a highly conserved manner, cells disassemble adhesion complexes, round up, and retract from their surroundings before division, suggestive of a primordial link between the cell cycle machinery and the regulation of cell adhesion to the ECM. In this study, we demonstrate that cyclin-dependent kinase 1 (CDK1) mediates this link. CDK1, in complex with cyclin A2, promotes adhesion complex and actin cytoskeleton organization during interphase and mediates a large increase in adhesion complex area as cells transition from G1 into S. Adhesion complex area decreases in G2, and disassembly occurs several hours before mitosis. This loss requires elevated cyclin B1 levels and is caused by inhibitory phosphorylation of CDK1–cyclin complexes. The inactivation of CDK1 is therefore the trigger that initiates remodeling of adhesion complexes and the actin cytoskeleton in preparation for rapid entry into mitosis.

scholarly journals Mechanical interplay between cell shape and actin cytoskeleton organization

Soft Matter ◽  
2020 ◽  
Vol 16 (27) ◽  
pp. 6328-6343 ◽  
Author(s):  
Koen Schakenraad ◽  
Jeremy Ernst ◽  
Wim Pomp ◽  
Erik H. J. Danen ◽  
Roeland M. H. Merks ◽  
...  
Keyword(s):  
Experimental Data ◽  
Theoretical Model ◽  
Actin Cytoskeleton ◽  
Cell Shape ◽  
Cytoskeleton Organization ◽  
Optical Micrograph ◽  
Adhesion Sites ◽  
Actin Cytoskeleton Organization

(Right) Optical micrograph (TRITC–Phalloidin) of a fibroblastoid cell. (Left) Configuration obtained from theoretical model using the adhesion sites of the experimental data as input.

scholarly journals Pan1p, End3p, and Sla1p, Three Yeast Proteins Required for Normal Cortical Actin Cytoskeleton Organization, Associate with Each Other and Play Essential Roles in Cell Wall Morphogenesis

2000 ◽  
Vol 20 (1) ◽  
pp. 12-25 ◽  
Author(s):  
Hsin-Yao Tang ◽  
Jing Xu ◽  
Mingjie Cai
Keyword(s):  
Cell Wall ◽  
Actin Cytoskeleton ◽  
Normal Cell ◽  
Cell Cortex ◽  
Repeat Region ◽  
Cortical Actin ◽  
Cytoskeleton Organization ◽  
Eh Domain ◽  
Actin Cytoskeleton Organization ◽  
Cell Wall Morphogenesis

ABSTRACT The EH domain proteins Pan1p and End3p of budding yeast have been known to form a complex in vivo and play important roles in organization of the actin cytoskeleton and endocytosis. In this report, we describe new findings concerning the function of the Pan1p-End3p complex. First, we found that the Pan1p-End3p complex associates with Sla1p, another protein known to be required for the assembly of cortical actin structures. Sla1p interacts with the first long repeat region of Pan1p and the N-terminal EH domain of End3p, thus leaving the Pan1p-End3p interaction, which requires the second long repeat of Pan1p and the C-terminal repeat region of End3p, undisturbed. Second, Pan1p, End3p, and Sla1p are also required for normal cell wall morphogenesis. Each of the Pan1-4, sla1Δ, andend3Δ mutants displays the abnormal cell wall morphology previously reported for the act1-1 mutant. These cell wall defects are also exhibited by wild-type cells overproducing the C-terminal region of Sla1p that is responsible for interactions with Pan1p and End3p. These results indicate that the functions of Pan1p, End3p, and Sla1p in cell wall morphogenesis may depend on the formation of a heterotrimeric complex. Interestingly, the cell wall abnormalities exhibited by these cells are independent of the actin cytoskeleton organization on the cell cortex, as they manifest despite the presence of apparently normal cortical actin cytoskeleton. Examination of several act1 mutants also supports this conclusion. These observations suggest that the Pan1p-End3p-Sla1p complex is required not only for normal actin cytoskeleton organization but also for normal cell wall morphogenesis in yeast.

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